Sequence-Defined Oligothioetheramides

Mintu Porel; Joseph S. Brown; Christopher A. Alabi

doi:10.1055/s-0034-1380113

Synlett, Inhaltsverzeichnis

Synlett 2015; 26(05): 565-571
DOI: 10.1055/s-0034-1380113

synpacts

Sequence-Defined Oligothioetheramides

Mintu Porel

Department of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853, USA eMail: caa238@cornell.edu

,

Joseph S. Brown

Department of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853, USA eMail: caa238@cornell.edu

,

Christopher A. Alabi*

Department of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853, USA eMail: caa238@cornell.edu

› Institutsangaben

Abstract

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Abstract

The importance of sequence-defined polymers is evident in highly developed biological systems. As such, their synthetic de novo production with similar macromolecular diversity, efficiency, and speed has been the focus of considerable research. In this brief review, the rationale behind the new synthesis of sequence-defined oligothioetheramides (oligoTEAs) will be placed in context with the accepted methods of peptide and peptoid synthesis, where all methods notably utilize chemical orthogonality in their design. Along with the conceptual design, we will discuss the assembly of oligoTEAs by highlighting the solution-phase kinetics of each orthogonal reaction, the liquid-phase fluorous purification methodology, a proof-of-principle synthesis, and the assembly of a full-length oligomer. Overall, the success of oligoTEAs stems from the rapid orthogonal chemical reactions at each end of the unique N-allyl-N-acrylamide monomer. OligoTEAs seek to contribute and advance the field of sequence-defined polymers by providing additional structural diversity to fundamentally study sequence-structure-function relationships for both material science and biological applications.

1 Introduction

2 Supported Synthesis via Orthogonal Chemistries

3 Conceptual Design of OligoTEA Assembly

4 Proof-of-Principle

5 Synthesis and Characterization of OligoTEAs

6 Conclusion

Key words

oligothioetheramide - sequence-defined - thiol-ene - orthogonal - polymer

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Referenzen

References
1 Lutz J, Ouchi M, Liu DR, Sawamoto M. Science 2013; 341: 1238149
2 Lee D, Redfern O, Orengo C. Nat. Rev. Mol. Cell Biol. 2007; 8: 995
3 Hudson WH, Ortlund EA. Nat. Rev. Mol. Cell Biol. 2014; 15: 749
4 Simon RJ, Kania RS, Zuckermann RN, Huebner DV, Jewell DA, Banville S, Ng S, Wang L, Rosenberg S, Marlowe CK. Proc. Natl. Acad. Sci. U.S.A. 1992; 89: 9367
5 Soth MJ, Nowick JS. Curr. Opin. Chem. Biol. 1997; 1: 120
6 Burkoth TS, Fafarman AT, Charych DH, Connolly MD, Zuckermann RN. J. Am. Chem. Soc. 2003; 125: 8841
7 Porel M, Alabi CA. J. Am. Chem. Soc. 2014; 136: 13162
8 Niu J, Hili R, Liu DR. Nat. Chem. 2013; 5: 282
9 Lewandowski B, De Bo G, Ward JW, Papmeyer M, Kuschel S, Aldegunde MJ, Gramlich PM. E, Heckmann D, Goldup SM, D’Souza DM, Fernandes AE, Leigh DA. Science 2013; 339: 189
10 Brudno Y, Liu DR. Chem. Biol. 2009; 16: 265
11 Minoda M, Sawamoto M, Higashimura T. Macromolecules 1990; 23: 4889
12 Nakatani K, Ogura Y, Koda Y, Terashima T, Sawamoto M. J. Am. Chem. Soc. 2012; 134: 4373
13 Satoh K, Ozawa S, Mizutani M, Nagai K, Kamigaito M. Nat. Commun. 2010; 1: 6
14 Zhang J, Matta ME, Hillmyer MA. ACS Macro Lett. 2012; 1: 1383
15 Ida S, Ouchi M, Sawamoto M. J. Am. Chem. Soc. 2010; 132: 14748
16 Zamfir M, Lutz J. Nat. Commun. 2012; 3: 1138
17 Pfeifer S, Lutz J. J. Am. Chem. Soc. 2007; 129: 9542
18 Gody G, Maschmeyer T, Zetterlund PB, Perrier S. Nat. Commun. 2013; 4: 2505
19 Merrifield RB. J. Am. Chem. Soc. 1963; 85: 2149
20 Beaucage SL, Caruthers MH. Tetrahedron Lett. 1981; 22: 1859
21 Beaucage SL, Iyer RP. Tetrahedron 1992; 48: 2223
22 Coin I, Beyermann M, Bienert M. Nat. Protoc. 2007; 2: 3247
23 Hartmann L, Krause E, Antonietti M, Börner HG. Biomacromolecules 2006; 7: 1239
24 Ponader D, Wojcik F, Beceren-Braun F, Dernedde J, Hartmann L. Biomacromolecules 2012; 13: 1845
25 Schaffert D, Badgujar N, Wagner E. Org. Lett. 2011; 13: 1586
26 Hahn F, Schepers U. J. Comb. Chem. 2008; 10: 267
27 Zuckermann RN. Biopolymers 2011; 96: 545
28 Bayer E, Mutter M. Nature (London) 1972; 237: 512
29 Han H, Wolfe MM, Brenner S, Janda KD. Proc. Natl. Acad. Sci. U.S.A. 1995; 92: 6419
30 Bonora GM, Scremin CL, Colonna FP, Garbesi A. Nucleic Acids Res. 1990; 18: 3155
31 Douglas SP, Whitfield DM, Krepinsky JJ. J. Am. Chem. Soc. 1991; 113: 5095
32 Solleder SC, Meier MA. R. Angew. Chem. Int. Ed. 2014; 53: 711
33 Atherton E, Clive DL. J, Sheppard RC. J. Am. Chem. Soc. 1975; 97: 6584
34 Atherton E, Logan CJ, Sheppard RC. J. Chem. Soc., Perkin Trans. 1 1981; 538
35 Wang S, Merrifield RB. J. Am. Chem. Soc. 1969; 91: 6488
36 Wang S. J. Am. Chem. Soc. 1973; 95: 1328
37 Matsueda GR, Stewart JM. Peptides 1981; 2: 45
38 Houghten RA, Ostresh JM, Klipstein FA. Eur. J. Biochem. 1984; 145: 157
39 Houghten RA. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 5131
40 Sarin VK, Kent SB. H, Merrifield RB. J. Am. Chem. Soc. 1980; 102: 5463
41 Mitchell AR, Mitchell ER, Kent SB. H, Engelhard M, Merrifield RB. J. Org. Chem. 1978; 43: 2845
42 Hood CA, Fuentes G, Patel H, Page K, Menakuru M, Park JH. J. Pept. Sci. 2008; 14: 97
43 Berndt P, Fields GB, Tirrell M. J. Am. Chem. Soc. 1995; 117: 9515
44 Wellings DA, Atherton E. Methods Enzymol. 1997; 289: 44
45 Atherton E, Fox H, Harkiss D, Logan CJ, Sheppard RC, Williams BJ. J. Chem. Soc., Chem. Commun. 1978; 537
46 Bacsa B, Desai B, Dibó G, Kappe CO. J. Pept. Sci. 2006; 12: 633
47 Hussein WM, Liu T, Toth I, Skwarczynski M. Org. Biomol. Chem. 2013; 11: 2370
48 Murray JK, Gellman SH. Nat. Protoc. 2007; 2: 624
49 Matsushita T, Hinou H, Kurogochi M, Shimizu H, Nishimura S. Org. Lett. 2005; 7: 877
50 Banerjee J, Hanson AJ, Muhonen WW, Shabb JB, Mallik S. Nat. Protoc. 2009; 5: 39
51 Figliozzi G, Goldsmith R, Ng S, Banville S. Methods Enzymol. 1996; 267: 437
52 Kirshenbaum K, Barron AE, Goldsmith RA, Arm P, Armand P, Bradley EK, Truong KT. V, Dill KA, Cohen FE, Zuckermann RN. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 4303
53 Holub JM, Jang H, Kirshenbaum K. Org. Biomol. Chem. 2006; 4: 1497
54 Murphy JE, Uno T, Hamer JD, Cohen FE, Dwarki V, Zuckermann RN. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 1517
55 Rosales AM, Murnen HK, Zuckermann RN, Segalman R. Macromolecules 2010; 43: 5627
56 Seo J, Michaelian N, Owens SC, Dashner ST, Wong AJ, Barron AE, Carrasco MR. Org. Lett. 2009; 11: 5210
57 Olivos HJ, Olivos OJ, Alluri PG, Reddy MM, Salony D, Kodadek T. Org. Lett. 2002; 4: 4057
58 Gorske BC, Jewell SA, Guerard EJ, Blackwell HE. Org. Lett. 2005; 7: 1521
59 Nnanabu E, Burgess K. Org. Lett. 2006; 8: 1259
60 Messeguer J, Cortés N, García-Sanz N, Navarro-Vendrell G, Ferrer-Montiel A, Messeguer A. J. Comb. Chem. 2008; 10: 974
61 Cho S, Choi J, Kim A, Lee Y, Kwon Y. J. Comb. Chem. 2010; 12: 321
62 Merrifield RB. Biochemistry 1964; 3: 1385
63 Kosuri S, Church GM. Nat. Methods 2014; 11: 499
64 Nucleic Acids Book: Solid-Phase Oligonucleotide Synthesis . Brown T, Brown TJr. ATDBio Ltd; Southampton: 2014
65 Peptide Antigens: A Practical Approach . Wisdom GB. Oxford University Press; Cary (NC, USA): 1994
66 Fillon Y. Dissertation. Purdue University; USA: 2007: 129
67 Bray BL. Nat. Rev. Drug Discovery 2003; 2: 587
68 Anderson GW, McGregor AC. J. Am. Chem. Soc. 1957; 79: 6180
69 Fields GB, Noble RL. Int. J. Pept. Protein Res. 1990; 35: 161
70 Carpino LA, Han GY. J. Am. Chem. Soc. 1970; 92: 5748
71 Zuckermann RN, Kerr JM, Kent SB. H, Moos WH. J. Am. Chem. Soc. 1992; 114: 10646
72 Sun J, Zuckermann RN. ACS Nano 2013; 7: 4715
73 Nam KT, Shelby SA, Choi PH, Marciel AB, Chen R, Tan L, Chu TK, Mesch RA, Lee B.-C, Connolly MD, Kisielowski C, Zuckermann RN. Nat. Mater. 2010; 9: 454
74 Chan JW, Hoyle CE, Lowe AB, Bowman M. Macromolecules 2010; 43: 6381
75 Chan JW, Hoyle CE, Lowe AB. J. Am. Chem. Soc. 2009; 131: 5751
76 Suga S, Kageyama Y, Babu G, Itami K, Yoshida J. Org. Lett. 2004; 6: 2709
77 Curran DP. Synlett 2001; 1488
78 Curran DP, Hadida S, He M. J. Org. Chem. 1997; 62: 6714